Interfacing formate dehydrogenase with metal oxides for reversible electrocatalysis and solar‐driven reduction of carbon dioxide

The integration of enzymes with synthetic materials allows efficient electrocatalysis and solar fuels production. Here, we couple formate dehydrogenase (FDH) from Desulfovibrio vulgaris Hildenborough (DvH) to metal oxides for catalytic CO2 reduction and report an in‐depth study of the resulting enzyme‐material interface. Protein film voltammetry (PFV) demonstrates stable binding of FDH on metal oxide electrodes and reveals reversible and selective reduction of CO2 to formate. Quartz crystal microbalance (QCM) and attenuated total reflection infrared (ATR IR) spectroscopy confirm a high binding affinity for FDH to the TiO2 surface. Adsorption of FDH on dye‐sensitized TiO2 allows for visible‐light driven CO2 reduction to formate in the absence of a soluble redox mediator with a turnover frequency (TOF) of 11 ± 1 s−1. The strong coupling of the enzyme to the semiconductor gives rise to a new benchmark in selective photoreduction of aqueous CO2 to formate.

from A via a.sfakia on Inoreader http://bit.ly/2DXl7Oy